Protein Stability §

Group: 4 #group-4

Relations §

• Disulfide Bridges: The formation of disulfide bridges increases the stability of proteins by introducing covalent cross-links between different parts of the polypeptide chain.
• Hydrophobic Interactions: Hydrophobic interactions contribute to the stability of proteins by burying non-polar residues in the protein core.
• Fold Resistance: Fold resistance is a measure of the stability of a protein’s folded state, which is determined by the balance between stabilizing and destabilizing forces.
• Protein Engineering: Improving protein stability is often a goal in protein engineering to enhance the protein’s shelf life and performance.
• Protein Folding: The folded structure of a protein is generally more stable than the unfolded state.
• Protein Folding Landscapes: The stability of a protein’s native state is determined by its position on the folding landscape.
• Protein Folding Models: Protein folding models are used to study the factors that contribute to protein stability.